I guess the take away is to not eat the same stuff every single day...

From Cordains newsletter a short while back..

Lysozyme from Egg Whites by Loren Cordain

In all three of my books, I have advocated egg consumption, particularly eggs that are produced with high omega 3 fatty acid contents. Chicken eggs are generally a nutritious food and are a good source of selenium, vitamin A, vitamin D and the B vitamins, some minerals and lutein as Barbara indicated. Additionally, numerous recent experimental and epidemiological studies (reviewed in references 1, 2) indicate that regular egg consumption (7 per week) does not increase the risk for coronary heart disease (CHD). As I have previously noted, although eggs are one of the most concentrated sources of dietary cholesterol (212 mg per egg), dietary cholesterol has a minimal effect upon blood cholesterol concentrations in most people1, 3. Further, high cholesterol egg diets cause an increase in blood HDL particles1 and reduce the highly atherogenic small dense LDL particles while simultaneously increasing the less atherogenic large, "fluffy" LDL particles4, 5.

So, should everybody include eggs in their diet on a daily basis? Not necessarily, particularly if we examine the evolutionary template. Without question our preagricultural ancestors would have collected and consumed eggs from birdsí nests whenever possible. However, in the wild, bird eggs only appear seasonally. Hence, pre-agricultural humans could have never consumed two eggs for breakfast every morning of the year similar to some westernized people, but rather only occasionally for a few brief weeks or months.

If we follow up on the clue from the evolutionary template and examine eggs more closely, they maintain certain nutritional shortcomings that may be problematic, particularly for people suffering from autoimmune diseases and allergies. Although eggs are classified as animal food sources and are lumped together with meats in the USDA My Pyramid, eggs are uniquely different from meats in that they represent the reproductive endpoints of adult birds which exist outside their motherís body in a semipermeable, warm compartment. As such, all eggs are particularly vulnerable to invasion, attack and destruction by microorganisms such as fungi, bacteria and viruses present in their nesting environment.

The innermost yolk of a chicken egg represents the growing embryo which is anchored to the albumen or egg white by structures called chalazae. Outward from the egg white are the inner and outer membranes and then the shell, all of which provide physical barriers to infection from pathogens and microorganisms. The egg white makes up about 58% of the total egg volume and contains about 50% of the total egg protein and is composed of 88.5% water, 10.5% protein and 0.5% carbohydrate6. The function of the egg white is threefold: 1) storage of nutrients for the growing embryo (yolk), 2) protection of the egg from microbial attack, and 3) transport of nutrients into the growing embryo.

As I have previously mentioned, a chicken egg is the reproductive endpoint for adult birds and survives by living outside its motherís body in a semi permeable compartment that is essentially immovable. Accordingly, it has no means of protecting itself from microorganisms or predation by physical escape or avoidance. For this reason, the evolutionary strategy eggs have taken to protect themselves from microbial invaders is to select for toxic substances in the egg white; mainly in the form of antimicrobial proteins. Table 1 lists the major proteins in egg whites and their likely functions.

Note that except for ovalbumen, which comprises 54% of the total protein in egg white, virtually all the other major proteins (~33% of the total) maintain one form or another of antimicrobial activity.

Egg white allergy in the general population varies between 1.6 Ė 3.2% and is the second most common cause of food allergy in children next to milk8. For both adults and children one or more of the following symptoms may occur: hives, atopic dermatitis (red, flaky itchy skin), asthma, runny nose, diarrhea, abdominal pain, rapid swelling of the skin and mucosa, and anaphylactic shock which may be life threatening. The major allergens in egg white are ovomucoid, ovalbumen, ovotransferrin and lysozyme8 (Table 1). So for the vast majority of children and adults (98.4 Ė 96.8% of the population), egg white allergy is not a problem, and except for anaphylactic shock is not a debilitating or life threatening condition.

The same conclusion may not be true for people suffering from an autoimmune disease (e.g. multiple sclerosis, rheumatoid arthritis, ankylosing spondylitis, lupus erythematosus and others), since egg white consumption may contribute to the origin and progression of these diseases via a process of molecular mimicry that I have previously outlined for dietary lectins found in wheat, peanuts and other grains and legumes11.

You can see from Table 1 that egg white protein is no simple protein, but rather a conglomeration of multiple proteins which have been designed by natural selection to cause toxic and lethal effects in bacteria and microorganisms reminiscent of food lectins found in grains and legumes11. In order for any food proteins to potentially cause or promote an autoimmune disease, it must:

1.Survive the human digestive processes intact
2.Cross the gut barrier intact either alone or with other attached proteins
3.Interact with the immune system in a manner suspected of causing an autoimmune disease.
A number of egg white proteins fulfill these necessary steps. Most problematic is the egg white protein, lysozyme which is actually an enzyme known as Nacetylhexosaminodase that is also found in many human tissues, including tears12. The function of lysozyme in both egg whites and in human tears is to act as a potent bacterialcidal agent by binding and dissolving bacterial cell walls12.

Bacterial cell walls are called the murein or peptidoglycan layer which is a gigantic polymer of (N-acetylglucosamine and N-acetylmuyramic acid) polysaccharide strands cross linked through short peptide bridges at the lactyl groups of the muramic acid residues. Lysozyme degrades bacterial cell walls by catalyzing hydrolysis of the beta (-1,4-) linkage between N-acetylglucosamine and N-acetylmuramic acid. Human cells do not maintain a murein (peptidoglycan) exterior lining. Consequently, dietary lysozyme from egg whites do no increase intestinal permeability by breakdown of intestinal cell membranes but rather lysozyme increases intestinal permeability by other means that I will explain. It is this increase in intestinal permeability or "leaky gut" that makes egg white consumption problematic for people with egg allergies or autoimmune disease.

Lysozyme is unusual among the major egg white proteins in that it has an alkaline isoelectric point, which means that it can form strong complexes with other egg white proteins including ovomucin, ovalbumen and ovotransferrin6, 12. Hence, even though lysozyme is a benign enzyme produced in our own bodies, when we eat egg white lysozyme, it comes as a compound attached to other egg white proteins or to gut borne bacterial proteins foreign to our bodies.

In the human digestive tract, enzymes called proteases normally break down proteins into their constituent amino acids so that the amino acids can be absorbed across the intestines. Because egg white protein contains high concentrations of protease inhibitors (ovomucoid, ovoinhibitor, ovostatin, cystatin - see Table 1), the human gut proteases (trypsin and chymotrypsin primarily) are less effective in degrading egg white proteins, and lysozyme/egg white protein complexes. Additionally lysozyme is stable in the acidic gut environment12 and therefore arrives intact in the lower gastrointestinal tract. It should also be mentioned that Lysozyme is heat stable, having been reported to withstand 100 degrees C with little loss of activity13. Matsuoka et al14 reported lysozyme to be stable in acidic solution (pH 4.5, 100 degree C for 3 min; pH 5.29, 100 degree C, 30 min. So lysozyme would survive any normal cooking procedures used for eggs.

So whatís wrong if lysozyme/egg white protein/bacterial complexes arenít dissolved by normal digestive processes? Normally, large multifaceted proteins such as these complexes donít have a prayer of getting across the intestinal barrier and into the bloodstream where they can interact with the immune system. Once again, lysozyme is an unusual protein because it rapidly breeches the gut barrier and enters human circulation15, due to its unusual chemical properties (a positively charged isoelectric point)16. Because lysozyme maintains a positive charge, it results in an electrostatic attraction to the negatively charged proteoglycans (the glycocalyx) of intestinal epithelial cells which in turn allows lysozyme to be absorbed rapidly into circulation16.

Absorption of pure egg white lysozyme by itself into circulation is likely not problematic because lysozyme is an enzyme that the body naturally produces. Rather it is the complexes that lysozyme forms with other egg white proteins, gut borne bacterial peptides and food peptides that may adversely stimulate the immune system. When these chimeric (monster) molecules breech the gut barrier via their net positive charge and enter circulation, they have the capacity to promote allergy and autoimmune disease.

Just how autoimmune diseases are triggered by gut borne antigens from egg white lysozyme and other common foods (cereal grains, legumes, dairy and certain saponin containing foods) is another good story that our research group has been working on for the past decade. We hope to publish this seminal paper in 2010.